scholarly journals Intrinsic Viscosity Measurements of Bovine Serum Albumin at Different Temperatures

Nature ◽  
1965 ◽  
Vol 205 (4969) ◽  
pp. 386-386 ◽  
Author(s):  
AMALA CHATTERJEE
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Intrinsic Viscosity ◽  
Bovine Serum ◽  
Viscosity Measurements ◽  
Different Temperatures

scholarly journals Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Martin Alberto Masuelli
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Intrinsic Viscosity ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Experimental Measurements ◽  
Viscosity Measurements ◽  
The Relationship

The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from the experimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interaction between the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when the concentration ranges from 0.2 to 36.71% wt. and the temperature from 35 to 40°C. The relationship between the concentration and intrinsic viscosity is determined according to the method of Huggins. The temperature increase reduces the ratio between inherent viscosity and concentration (ηi/c). This is reflected in the Van't Hoff curve. Furthermore, this work proposes hydrodynamic cohesion value as an indicator of the degree of affinity of protein with water and thermodynamic implications in conformational changes.

scholarly journals Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

scholarly journals Spectroscopic Studies of the Interaction between Metformin Hydrochloride and Bovine Serum Albumin

2012 ◽  
Vol 11 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Ahmad Tanwir ◽  
Rahat Jahan ◽  
Mohiuddin Abdul Quadir ◽  
Mohammad A Kaisar ◽  
Md Khalid Hossain
Keyword(s):  
Hydrogen Bond ◽  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies ◽  
Metformin Hydrochloride ◽  
Tryptophan Residue ◽  
Different Temperatures ◽  
Hoff Equation

The affinity of a drug to serum albumin has influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of metformin hydrochloride (MET) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under different conditions. It was observed that the fluorescence  quenching of BSA by metformin hydrochloride is a result of the formation of metformin hydrochloride- BSA complex with probable involvement of tryptophan residue. Fluorescence quenching constants were determined using  the Stern- Volmer equation and Van’t Hoff equation to provide a measure of the thermodynamic parameters ?G, ?H, and ?S at different temperatures indicating that the hydrogen bond and the hydrophobic forces play a major role for metformin hydrochloride- BSA association. DOI: http://dx.doi.org/10.3329/dujps.v11i1.12486 Dhaka Univ. J. Pharm. Sci. 11(1): 45-49, 2012 (June)

scholarly journals Insight into the Interaction between the HIV-1 Integrase Inhibitor Elvitegravir and Bovine Serum Albumin: A Spectroscopic Study

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Ali Saber Abdelhameed
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Absorption Spectra ◽  
Bovine Serum ◽  
Average Distance ◽  
Three Dimensional ◽  
Integrase Inhibitor ◽  
Visible Absorption ◽  
Spontaneous Interaction ◽  
Different Temperatures

The interaction between the anti-HIV drug Elvitegravir (EVG) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and UV-visible absorption spectra. The mechanism for quenching the fluorescence of BSA by EVG is discussed. It was found that EVG can quench the intrinsic fluorescence of BSA through a static quenching procedure. The quenching type, association constant, and number of binding sites were investigated. The binding constant of EVG with BSA was calculated at different temperatures based on fluorescence quenching results. The thermodynamic parametersΔHθ,ΔGθ, andΔSθwere determined. The positiveΔSθand negativeΔHθandΔGθvalues showed that a spontaneous interaction may involve both roles of hydrophobic interaction and hydrogen bonding. The interaction of BSA with EVG was also confirmed by UV absorption spectra. The average distance,r, between donor (BSA) and acceptor (EVG) was obtained according to Förster’s theory of nonradiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the conformational change of BSA molecules that occur upon addition of EVG and showed, upon binding, a possibility of increasing hydrophobicity around tryptophan residues of BSA.

Interaction of Nitroglycerin with Bovine Serum Albumin and the Influence of Metal Ions on the Binding

2020 ◽  
Vol 42 (2) ◽  
pp. 180-180
Author(s):  
Chengman Bao Chengman Bao ◽  
Jialian Wang Jialian Wang ◽  
Xuehong Tong Xuehong Tong ◽  
Chunli Zhang Chunli Zhang ◽  
Xinhui Tang Xinhui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Binding Constants ◽  
Entropy Change ◽  
Quenching Rate ◽  
Different Temperatures ◽  
Quenching Rate Constant ◽  
Bimolecular Quenching

The effect of Cu2+, Ca2+, Mg2+and Zn2+ on the interaction between nitroglycerin and bovine serum albumin was investigated. The bimolecular quenching rate constant, the Stern-Volmer quenching constant, the binding constants and the number of binding sites were calculated in the absence and presence of Cu2+, Ca2+, Mg2+and Zn2+. The quenching constants of nitroglycerin to bovine serum albumin were increased in the presence of metal ions. Static quenching mechanism was also confirmed. The binding constants of nitroglycerin to bovine serum albumin were influenced by different metal ions. The enthalpy change, free energy chang, entropy change and the distance between the donor and the acceptor at different temperatures were calculated. The results indicated that energy transfer from bovine serum albumin to nitroglycerin occurs with high probability.

Temperature- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) microgels as a carrier for controlled protein adsorption and release

Soft Matter ◽  
2021 ◽  
Author(s):  
Priyanshi Agnihotri ◽  
Sangeeta Jangra ◽  
Shikha Aery ◽  
Abhijit Dan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Adsorption ◽  
Methacrylic Acid ◽  
Bovine Serum ◽  
Ph Responsive ◽  
Ph Values ◽  
Different Temperatures ◽  
Adsorption And Release

Herein, we report controlled protein adsorption and delivery of thermo- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) (PNIPAM-co-MAA) microgels at different temperatures, pH values and ionic strengths by employing bovine serum albumin (BSA)...

scholarly journals Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Baosheng Liu ◽  
Chao Yang ◽  
Xiaona Yan ◽  
Jing Wang ◽  
Yunkai Lv
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Electrostatic Force ◽  
Binding Constants ◽  
Amino Acid Residues ◽  
Synchronous Fluorescence Spectra ◽  
Different Temperatures ◽  
Order Of Magnitude

The interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants (Ka) was 104, and the number of binding site (n) in the binary system was approximately equal to 1. The binding distance (r) was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied.

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